5E6G
Crystal Structure of De Novo Designed Protein CA01
Summary for 5E6G
| Entry DOI | 10.2210/pdb5e6g/pdb |
| Descriptor | De novo designed protein CA01, PHOSPHATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | computational design, protein engineering, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 2 |
| Total formula weight | 31435.07 |
| Authors | Jacobs, T.M.,Williams, T.,Kuhlman, B. (deposition date: 2015-10-09, release date: 2016-05-18, Last modification date: 2024-03-06) |
| Primary citation | Jacobs, T.M.,Williams, B.,Williams, T.,Xu, X.,Eletsky, A.,Federizon, J.F.,Szyperski, T.,Kuhlman, B. Design of structurally distinct proteins using strategies inspired by evolution. Science, 352:687-690, 2016 Cited by PubMed Abstract: Natural recombination combines pieces of preexisting proteins to create new tertiary structures and functions. We describe a computational protocol, called SEWING, which is inspired by this process and builds new proteins from connected or disconnected pieces of existing structures. Helical proteins designed with SEWING contain structural features absent from other de novo designed proteins and, in some cases, remain folded at more than 100°C. High-resolution structures of the designed proteins CA01 and DA05R1 were solved by x-ray crystallography (2.2 angstrom resolution) and nuclear magnetic resonance, respectively, and there was excellent agreement with the design models. This method provides a new strategy to rapidly create large numbers of diverse and designable protein scaffolds. PubMed: 27151863DOI: 10.1126/science.aad8036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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